id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-000574-7eflwyxk	Liu, Yanli	Effects of a Non-Conservative Sequence on the Properties of β-glucuronidase from Aspergillus terreus Li-20	2012-02-07		.txt	text/plain	3919	216	52	The non-conservative N-terminal domain of the protein phosphatase1 (PP1), with 1-8 residues deleted, showed higher sensitivity to three substrates and influenced the structure and properties of PP1 [10] , whereas the truncation of the Cterminal region improved the thermal stability of endo-bglucanase from Bacillus subtilis JA18 [11] . The TIM barrel domain, which is one of the most common catalytic domains, is adopted by about 10% of the enzymes; thus, sequence modification inside or outside the domain to improve the enzymatic property and determine the catalytic mechanism was reported in many studies. In the present research, Atgus and the partial sequence [Atgus(-3t)] without Cterminal non-conservative sequence behind the TIM barrel domain were amplified in order to investigate effects of nonconservative sequence on enzymatic property. Based on the same hydrolyzing mode, relatively higher thermal stability, and especially the enhanced affinity and catalytic efficiency for GL, deletion of the non-conservative sequence behind the TIM barrel domain was a successful evolution of AtGUS.	./cache/cord-000574-7eflwyxk.txt	./txt/cord-000574-7eflwyxk.txt